DPP2_RAT
ID DPP2_RAT Reviewed; 500 AA.
AC Q9EPB1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dipeptidyl peptidase 2;
DE EC=3.4.14.2;
DE AltName: Full=Dipeptidyl aminopeptidase II;
DE AltName: Full=Dipeptidyl peptidase 7;
DE AltName: Full=Dipeptidyl peptidase II;
DE Short=DPP II;
DE AltName: Full=Quiescent cell proline dipeptidase;
DE Flags: Precursor;
GN Name=Dpp7; Synonyms=Dpp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=11173530; DOI=10.1093/oxfordjournals.jbchem.a002855;
RA Araki H., Li Y.-H., Yamamoto Y., Haneda M., Nishi K., Kikkawa R.,
RA Ohkubo I.;
RT "Purification, molecular cloning, and immunohistochemical localization of
RT dipeptidyl peptidase II from the rat kidney and its identity with quiescent
RT cell proline dipeptidase.";
RL J. Biochem. 129:279-288(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=11139392; DOI=10.1042/0264-6021:3530283;
RA Fukasawa K.M., Fukasawa K., Higaki K., Shiina N., Ohno M., Ito S.,
RA Otogoto J., Ota N.;
RT "Cloning and functional expression of rat kidney dipeptidyl peptidase II.";
RL Biochem. J. 353:283-290(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 67-72; 123-133; 157-184; 214-225; 264-273; 416-437 AND
RP 459-480, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the degradation of some
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially
CC when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially
CC tripeptides.; EC=3.4.14.2;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Lysosome. Cytoplasmic vesicle {ECO:0000250}.
CC Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney, but also
CC expressed in a variety of tissues.
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; AB048711; BAB13500.1; -; mRNA.
DR EMBL; AB038232; BAB11691.1; -; mRNA.
DR EMBL; BC078783; AAH78783.1; -; mRNA.
DR PIR; JC7668; JC7668.
DR RefSeq; NP_114179.1; NM_031973.1.
DR AlphaFoldDB; Q9EPB1; -.
DR SMR; Q9EPB1; -.
DR IntAct; Q9EPB1; 1.
DR STRING; 10116.ENSRNOP00000017271; -.
DR BindingDB; Q9EPB1; -.
DR ChEMBL; CHEMBL4352; -.
DR ESTHER; ratno-dpp2; Prolylcarboxypeptidase.
DR MEROPS; S28.002; -.
DR GlyGen; Q9EPB1; 6 sites, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9EPB1; -.
DR jPOST; Q9EPB1; -.
DR PaxDb; Q9EPB1; -.
DR PRIDE; Q9EPB1; -.
DR Ensembl; ENSRNOT00000017271; ENSRNOP00000017271; ENSRNOG00000012640.
DR GeneID; 83799; -.
DR KEGG; rno:83799; -.
DR UCSC; RGD:71073; rat.
DR CTD; 29952; -.
DR RGD; 71073; Dpp7.
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000159838; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; Q9EPB1; -.
DR OMA; IKGGAHH; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; Q9EPB1; -.
DR TreeFam; TF314414; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9EPB1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012640; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q9EPB1; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:RGD.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasmic vesicle; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..36
FT /id="PRO_0000027318"
FT CHAIN 37..500
FT /note="Dipeptidyl peptidase 2"
FT /id="PRO_0000027319"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 453
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 55114 MW; 401089D282CE1514 CRC64;
MGLHPCSPVD HGVPSWVLVL LLTLGLCSLQ ATADSVLDPD FRENYFEQYM DHFNFESFSN
KTFGQRFLVS DKFWKMGEGP IFFYTGNEGD IWSLANNSGF IVELAAQQEA LLVFAEHRYY
GKSLPFGVQS TQRGYTQLLT VEQALADFAV LLQALRHNLG VQDAPTIAFG GSYGGMLSAY
MRMKYPHLVA GALAASAPVI AVAGLGNPDQ FFRDVTADFY GQSPKCAQAV RDAFQQIKDL
FLQGAYDTIS QNFGTCQSLS SPKDLTQLFG FARNAFTVLA MMDYPYPTNF LGPLPANPVK
VGCERLLSEG QRIMGLRALA GLVYNSSGME PCFDIYQMYQ SCADPTGCGT GSNARAWDYQ
ACTEINLTFD SNNVTDMFPE IPFSDELRQQ YCLDTWGVWP RPDWLQTSFW GGDLKAASNI
IFSNGDLDPW AGGGIQRNLS TSIIAVTIQG GAHHLDLRAS NSEDPPSVVE VRKLEATLIR
EWVAAARLKQ PAEAQWPGPK
